Physical chemical studies will be carried out on the bacterial redox proteins, azurin, cyt c551 and cyt cd1 oxidase and on transferrin, the serum iron transport protein. The proton NMR study of apoazurin from Alcaligenes faecalis will be carried out. A T-jump study will be made of c551 from Pseudomonas aeruginosa. Photoionization experiments will be carried out on several blue copper proteins including plastocyanin and ceruloplasmin. An attempt will be made to purify cyt cd1 oxidase from a flavin contaminant so that its resonance Roman spectrum can be measured. The 7Fo yields 5Do absorption of Eu3 plus or minus transferrin (monitored by laser induced fluorescence) will be studied in detail to see if it can be resolved into two components, one for each binding site. If this resolution is possible, it is planned to analyze a number of human serum samples to see if there is a preference for occupation of one or the other site.